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Information on EC 3.1.22.1 - deoxyribonuclease II and Organism(s) Mus musculus and UniProt Accession P56542
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3.1.22.1 deoxyribonuclease IISpecify your search results
Word Map
- 3.1.22.1
- chromatin
- endonuclease
- nuclei
- spleen
- nucleases
- nucleosome
- cathepsins
-
micrococcal
-
engulf
-
caspase-independent
- spiralis
- medicine
- trichinella
-
caspase-activated
- dnaase
-
ii-like
-
internucleosomal
-
undigested
-
endonucleolytic
-
nonhistone
-
corpses
-
cation-independent
- analysis
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
dnase ii, nuc-1, acid dnase, deoxyribonuclease ii, l-dnase ii, acid deoxyribonuclease, lei/l-dnase ii, dnase iialpha, dnase iibeta, dnase 2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acid deoxyribonuclease
-
-
-
-
acid DNase
deoxyribonucleate 3'-nucleotidohydrolase
-
-
-
-
DNase II
DNase IIbeta
lysosomal DNase II
-
-
-
-
pancreatic DNase II
-
-
-
-
R31240_2
-
-
-
-
acid DNase
-
-
-
-
DNase II
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products
deoxyribonuclease IIbeta is a protein with considerably homology to DNase II
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9025-64-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
supercoiled plasmid DNA + H2O
relaxed plasmid DNA + ?
-
plasmid pBR322
primary reaction product, "nicking" mechanism
?
additional information
?
-
-
the enzyme is required for degrading DNA of dying cells and this function is necessary for the proper removal of apoptotic nuclei during fetal development
-
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
-
-
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
-
-
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
the enzyme in macrophages appears to be responsible for destroying the nuclear DNA expelled from erythroid precursor cells
-
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
it is proposed that DNase II together with the Chk2, p53, and p21 pathway forms a genetic barrier blocking the replication of potentially harmful DNA introduced via apoptotic bodies, thereby preventing transformation and malignant development
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the enzyme is required for degrading DNA of dying cells and this function is necessary for the proper removal of apoptotic nuclei during fetal development
-
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
the enzyme in macrophages appears to be responsible for destroying the nuclear DNA expelled from erythroid precursor cells
-
?
DNA + H2O
3'-phosphooligonucleotides + 5'-hydroxyoligonucleotides
-
it is proposed that DNase II together with the Chk2, p53, and p21 pathway forms a genetic barrier blocking the replication of potentially harmful DNA introduced via apoptotic bodies, thereby preventing transformation and malignant development
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
growth hormone
-
in mice fed a 20% protein diet, growth hormone treatment decreases elevated activites of DNase II and RNase
-
human growth hormone
-
treatment of post-weaning mice results in 63% inhibition in gastrocnemius muscle
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
isoform DNase II and acid RNase directly participate in muscle DNA and RNA degradation. Treatment with recombinant human growth hormone leads to 63% inhibition of DNase and 48% inhibition of RNase activity
additional information
-
isoform DNase IIbeta accounts for about 50% of the acid nuclease activity in cortical fiber cell. Activity is strongest in early differentiation and associated with the lysosomal fraction. Later, an increasing portion of enzyme is found in cytosol
-
the enzyme gene is expressed in the fetal liver of the wild-type and DNase II+/- embryos, but not in the DNase II-/- liver
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
during early differentiation, localization to lysosome. Later, an increasing portion of enzyme is found in cytosol
-
DNase IIbeta resides in the lysosomes of cortical fiber cells, close to the organelle-free zone
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and heterophagolysosome of macrophages and mononuclear cells, two bands with strong immunoreactivity appear at molecular masses of 30 and 23 kDa
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
key role of DNase II in DNA sensing by the DNA sensor Toll-like receptor 9 (TLR9). DNase II is required for TLR9 activation by bacterial genomic DNA. TLR9 responds to DNA fragments generated by DNase II
physiological function
physiological function
-
fundamental role in the degradation of DNA from both apoptotic cells, and nuclei extruded from red blood cells during erythropoiesis; mice lacking DNase II die late in embryogenesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DNS2A_MOUSE
353
0
38811
Swiss-Prot
Secretory Pathway (Reliability: 1)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
protein is synthesized as a precursor with a signal sequence
proteolytic modification
-
processing of DNase II in vivo is greatly altered in the liver of mice lacking cathepsin L. DNase II is extracellularly secreted from cells overexpressing DNase II and is detected as a pro-form, which is activated under acidic conditions. In transgenic COS1 cells, a band of 45 kDa colocalizeswith ER marker protein Bip and two bands with strong immunoreactivity appear at molecular masses of 30 and 23 kDa in lysosomes
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
DNase IIdeficient mouse embryos accumulate undigested DNA in macrophages, which are present in all tissues, such as the thymus, kidney, interdigit, spleen, and liver. The accumulation of undegraded DNA also stimulates production of interferon-beta, and eventually causes death of the knockout mice. Peripheral blood of DNase II-/- embryos contain massive nucleated erythrocytes and no live DNase II-/- mice are born because of severe respiratory disturbance. Deficiency of the DNase II in adult mice is not lethal
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the subsequent targeted disruption of the DNase II gene confirms the requirement of DNase II activity within phagocytic cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
DNase II in macrophage lysosomes is responsible for definitive erythropoiesis in mouse fetal liver
medicine
-
is involved in apoptosis, LEI/LDNase II is activated mostly after metabolic stress
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Baker, K.P.; Baron, W.F.; Henzel, W.J.; Spencer, S.A.
Molecular cloning and characterization of human and murine DNase II
Gene
215
281-289
1998
Homo sapiens, Mus musculus, Sus scrofa
Georgatsos, J.G.
Bond-cleaving specificity of a deoxyribonuclease II from mouse mammary tumors
Biochim. Biophys. Acta
142
128-132
1967
Mus musculus
Krieser, R.J.; MacLea, K.S.; Longnecker, D.S.; Fields, J.L.; Fiering, S.; Eastman, A.
Deoxyribonuclease IIalpha is required during the phagocytic phase of apoptosis and its loss causes perinatal lethality
Cell Death Differ.
9
956-962
2002
Mus musculus
Krieser, R.J.; MacLea, K.S.; Park, J.P.; Eastman, A.
The cloning, genomic structure, localization, and expression of human deoxyribonuclease IIbeta
Gene
269
205-216
2001
Homo sapiens (Q8WZ79), Homo sapiens, Mus musculus
MacLea, K.S.; Krieser, R.J.; Eastman, A.
A family history of deoxyribonuclease II: surprises from Trichinella spiralis and Burkholderia pseudomallei
Gene
305
1-12
2003
Bos taurus (P56541), Caenorhabditis elegans (P34387), Caenorhabditis elegans (P34508), Caenorhabditis elegans (Q17778), Caenorhabditis elegans, Caenorhabditis elegans F09G8.2 (P34387), Caenorhabditis elegans K04H4.6 (P34508), Caenorhabditis elegans NUC-1 (Q17778), Drosophila melanogaster (Q7JYM9), Homo sapiens (O00115), Homo sapiens (Q8WZ79), Homo sapiens, Mus musculus (P56542), Mus musculus (Q9QY48), Rattus norvegicus (Q9QZK8), Rattus norvegicus (Q9QZK9), Sus scrofa (O62855)
Evans, C.J.; Aguilera, R.J.
DNase II: genes, enzymes and function
Gene
322
1-15
2003
Caenorhabditis elegans, Caenorhabditis elegans NUC-1, Drosophila melanogaster, Homo sapiens, Mus musculus
Kawane, K.; Fukuyama, H.; Kondoh, G.; Takeda, J.; Ohsawa, Y.; Uchiyama, Y.; Nagata, S.
Requirement of DNase II for definitive erythropoiesis in the mouse fetal liver
Science
292
1546-1549
2001
Mus musculus
Bergsmedh, A.; Ehnfors, J.; Kawane, K.; Motoyama, N.; Nagata, S.; Holmgren, L.
DNase II and the Chk2 DNA damage pathway form a genetic barrier blocking replication of horizontally transferred DNA
Mol. Cancer Res.
4
187-195
2006
Mus musculus
Lopez-Oliva, M.E.; Agis-Torres, A.; Marquez, E.; Munoz-Martinez, E.
Growth hormone modulates the degradative capacity of muscle nucleases but not of cathepsin D in post-weaning mice
Comp. Biochem. Physiol. A
148A
159-167
2007
Mus musculus
-
Nakahara, M.; Nagasaka, A.; Koike, M.; Uchida, K.; Kawane, K.; Uchiyama, Y.; Nagata, S.
Degradation of nuclear DNA by DNase II-like acid DNase in cortical fiber cells of mouse eye lens
FEBS J.
274
3055-3064
2007
Mus musculus
Lopez-Oliva, M.E.; Agis-Torres, A.; Munoz-Martinez, E.
The modulator effect of GH on skeletal muscle lysosomal enzymes is dietary protein dependent
Growth Horm. IGF Res.
17
137-148
2007
Mus musculus
De Maria, A.; Bassnett, S.
DNase IIbeta distribution and activity in the mouse lens
Invest. Ophthalmol. Vis. Sci.
48
5638-5646
2007
Mus musculus
Torriglia, A.; Lepretre, C.; Padron-Barthe, L.; Chahory, S.; Martin, E.
Molecular mechanism of L-DNase II activation and function as a molecular switch in apoptosis
Biochem. Pharmacol.
76
1490-1502
2008
Gallus gallus, Cricetulus griseus, Homo sapiens, Mus musculus, Rattus norvegicus
Liu, M.F.; Wu, X.P.; Wang, X.L.; Yu, Y.L.; Wang, W.F.; Chen, Q.J.; Boireau, P.; Liu, M.Y.
The functions of Deoxyribonuclease II in immunity and development
DNA Cell Biol.
27
223-228
2008
Acanthaster planci, Drosophila sp. (in: flies), Haemonchus contortus, Homo sapiens, Mus musculus, Sus scrofa, Trichinella spiralis
Crow, Y.J.
The story of DNase II: a stifled death-wish leads to self-harm
Eur. J. Immunol.
40
2376-2378
2010
Mus musculus
Fischer, H.; Scherz, J.; Szabo, S.; Mildner, M.; Benarafa, C.; Torriglia, A.; Tschachler, E.; Eckhart, L.
DNase 2 is the main DNA-degrading enzyme of the stratum corneum
PLoS ONE
6
e17581
2011
Homo sapiens, Mus musculus
Ohkouchi, S.; Shibata, M.; Sasaki, M.; Koike, M.; Safig, P.; Peters, C.; Nagata, S.; Uchiyama, Y.
Biogenesis and proteolytic processing of lysosomal DNase II
PLoS ONE
8
e59148
2013
Mus musculus
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